HEADER TRANSLATION/ANTIBIOTIC 17-JUL-12 4G5G
TITLE EF-TU (ESCHERICHIA COLI) COMPLEXED WITH NVP-LDU796
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ELONGATION FACTOR TU 1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: EF-TU 1, P-43;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: THIOMURACIN A DERIVATIVE;
COMPND 8 CHAIN: I;
COMPND 9 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;
SOURCE 3 ORGANISM_TAXID: 83333;
SOURCE 4 STRAIN: K12;
SOURCE 5 GENE: TUFA, B3339, JW3301;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 MOL_ID: 2;
SOURCE 9 SYNTHETIC: YES;
SOURCE 10 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;
SOURCE 11 ORGANISM_TAXID: 32630
KEYWDS ELONGATION FACTOR, TRANSLATION-ANTIBIOTIC COMPLEX
EXPDTA X-RAY DIFFRACTION
AUTHOR D.PALESTRANT
REVDAT 1 26-DEC-12 4G5G 0
JRNL AUTH M.J.LAMARCHE,J.A.LEEDS,J.DZINK-FOX,E.GANGL,P.KRASTEL,
JRNL AUTH 2 G.NECKERMANN,D.PALESTRANT,M.A.PATANE,E.M.RANN,S.TIAMFOOK,
JRNL AUTH 3 D.YU
JRNL TITL ANTIBIOTIC OPTIMIZATION AND CHEMICAL STRUCTURE STABILIZATION
JRNL TITL 2 OF THIOMURACIN A.
JRNL REF J.MED.CHEM. V. 55 6934 2012
JRNL REFN ISSN 0022-2623
JRNL PMID 22812377
JRNL DOI 10.1021/JM300783C
REMARK 2
REMARK 2 RESOLUTION. 2.30 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : CNX
REMARK 3 AUTHORS : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-
REMARK 3 : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,
REMARK 3 : READ,RICE,SIMONSON,WARREN
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 50.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 2.000
REMARK 3 DATA CUTOFF HIGH (ABS(F)) : NULL
REMARK 3 DATA CUTOFF LOW (ABS(F)) : NULL
REMARK 3 COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 NUMBER OF REFLECTIONS : 21195
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : NULL
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : NULL
REMARK 3 R VALUE (WORKING SET) : 0.212
REMARK 3 FREE R VALUE : 0.258
REMARK 3 FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT : 952
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL
REMARK 3
REMARK 3 FIT/AGREEMENT OF MODEL WITH ALL DATA.
REMARK 3 R VALUE (WORKING + TEST SET, NO CUTOFF) : NULL
REMARK 3 R VALUE (WORKING SET, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL
REMARK 3 FREE R VALUE TEST SET COUNT (NO CUTOFF) : NULL
REMARK 3 ESTIMATED ERROR OF FREE R VALUE (NO CUTOFF) : NULL
REMARK 3 TOTAL NUMBER OF REFLECTIONS (NO CUTOFF) : 21195
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : NULL
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : NULL
REMARK 3 BIN RESOLUTION RANGE LOW (A) : NULL
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : NULL
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : NULL
REMARK 3 BIN R VALUE (WORKING SET) : NULL
REMARK 3 BIN FREE R VALUE : NULL
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : NULL
REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3099
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 35
REMARK 3 SOLVENT ATOMS : 117
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : NULL
REMARK 3 B22 (A**2) : NULL
REMARK 3 B33 (A**2) : NULL
REMARK 3 B12 (A**2) : NULL
REMARK 3 B13 (A**2) : NULL
REMARK 3 B23 (A**2) : NULL
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM SIGMAA (A) : NULL
REMARK 3 LOW RESOLUTION CUTOFF (A) : NULL
REMARK 3
REMARK 3 CROSS-VALIDATED ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM C-V LUZZATI PLOT (A) : NULL
REMARK 3 ESD FROM C-V SIGMAA (A) : NULL
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.009
REMARK 3 BOND ANGLES (DEGREES) : 1.60
REMARK 3 DIHEDRAL ANGLES (DEGREES) : NULL
REMARK 3 IMPROPER ANGLES (DEGREES) : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL MODEL : NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. RMS SIGMA
REMARK 3 MAIN-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN BOND (A**2) : NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE (A**2) : NULL ; NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELING.
REMARK 3 METHOD USED : NULL
REMARK 3 KSOL : NULL
REMARK 3 BSOL : NULL
REMARK 3
REMARK 3 NCS MODEL : NULL
REMARK 3
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 4G5G COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-OCT-12.
REMARK 100 THE RCSB ID CODE IS RCSB073761.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-MAR-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 8.23
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 17-ID
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.00000
REMARK 200 MONOCHROMATOR : SI
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 210
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 21195
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 2.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 1D8T
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.85
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.50
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS, 0.2M MGSO4, 24% PEG3350 ,
REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K, PH 8.23
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X+1/2,Y+1/2,-Z
REMARK 290 4555 X+1/2,-Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 40.15250
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 61.78850
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 40.15250
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 61.78850
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, I
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 MG MG A 503 LIES ON A SPECIAL POSITION.
REMARK 375 HOH A 689 LIES ON A SPECIAL POSITION.
REMARK 400
REMARK 400 COMPOUND
REMARK 400
REMARK 400 THE THIOMURACIN A DERIVATIVE IS OLIGOPEPTIDE, A MEMBER OF
REMARK 400 ANTIBIOTIC CLASS.
REMARK 400
REMARK 400 GROUP: 1
REMARK 400 NAME: THIOMURACIN A DERIVATIVE
REMARK 400 CHAIN: I
REMARK 400 COMPONENT_1: PEPTIDE LIKE POLYMER
REMARK 400 DESCRIPTION: NULL
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 0
REMARK 465 ALA A 1
REMARK 465 LYS A 2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3
REMARK 500 PRO A 128 C - N - CA ANGL. DEV. = 9.4 DEGREES
REMARK 500 TYR I 906 CB - CG - CD2 ANGL. DEV. = -4.0 DEGREES
REMARK 500 TYR I 906 CG - CD2 - CE2 ANGL. DEV. = -5.2 DEGREES
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: TORSION ANGLES
REMARK 500
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)
REMARK 500
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400
REMARK 500
REMARK 500 M RES CSSEQI PSI PHI
REMARK 500 LYS A 4 43.25 -98.69
REMARK 500 ALA A 57 -77.96 -89.35
REMARK 500 ASP A 142 75.61 -68.51
REMARK 500 GLU A 143 -13.04 -42.46
REMARK 500 ASP A 181 102.99 -53.21
REMARK 500 GLU A 215 -77.29 -107.63
REMARK 500 SER A 221 118.01 -38.78
REMARK 500 ILE A 247 -68.95 66.02
REMARK 500 ARG A 262 -1.27 74.94
REMARK 500 ARG A 333 -83.59 60.80
REMARK 500 H14 I 904 -32.77 -138.78
REMARK 500
REMARK 500 REMARK: NULL
REMARK 525
REMARK 525 SOLVENT
REMARK 525
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE
REMARK 525 NUMBER; I=INSERTION CODE):
REMARK 525
REMARK 525 M RES CSSEQI
REMARK 525 HOH A 690 DISTANCE = 5.90 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 501 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 25 OG1
REMARK 620 2 GDP A 502 O2B 80.5
REMARK 620 3 HOH A 615 O 171.9 92.0
REMARK 620 4 HOH A 601 O 79.0 81.2 96.8
REMARK 620 5 HOH A 602 O 83.7 84.3 98.8 159.0
REMARK 620 6 HOH A 616 O 82.9 163.2 104.7 98.4 91.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 503 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HOH A 654 O
REMARK 620 2 HOH A 653 O 101.6
REMARK 620 3 HOH A 681 O 113.0 84.2
REMARK 620 N 1 2
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR CHAIN I OF THIOMURACIN A
REMARK 800 DERIVATIVE
DBREF 4G5G A 2 393 UNP P0CE47 EFTU1_ECOLI 3 394
DBREF 4G5G I 900 912 PDB 4G5G 4G5G 900 912
SEQADV 4G5G MET A 0 UNP P0CE47 EXPRESSION TAG
SEQADV 4G5G ALA A 1 UNP P0CE47 EXPRESSION TAG
SEQRES 1 A 394 MET ALA LYS GLU LYS PHE GLU ARG THR LYS PRO HIS VAL
SEQRES 2 A 394 ASN VAL GLY THR ILE GLY HIS VAL ASP HIS GLY LYS THR
SEQRES 3 A 394 THR LEU THR ALA ALA ILE THR THR VAL LEU ALA LYS THR
SEQRES 4 A 394 TYR GLY GLY ALA ALA ARG ALA PHE ASP GLN ILE ASP ASN
SEQRES 5 A 394 ALA PRO GLU GLU LYS ALA ARG GLY ILE THR ILE ASN THR
SEQRES 6 A 394 SER HIS VAL GLU TYR ASP THR PRO THR ARG HIS TYR ALA
SEQRES 7 A 394 HIS VAL ASP CYS PRO GLY HIS ALA ASP TYR VAL LYS ASN
SEQRES 8 A 394 MET ILE THR GLY ALA ALA GLN MET ASP GLY ALA ILE LEU
SEQRES 9 A 394 VAL VAL ALA ALA THR ASP GLY PRO MET PRO GLN THR ARG
SEQRES 10 A 394 GLU HIS ILE LEU LEU GLY ARG GLN VAL GLY VAL PRO TYR
SEQRES 11 A 394 ILE ILE VAL PHE LEU ASN LYS CYS ASP MET VAL ASP ASP
SEQRES 12 A 394 GLU GLU LEU LEU GLU LEU VAL GLU MET GLU VAL ARG GLU
SEQRES 13 A 394 LEU LEU SER GLN TYR ASP PHE PRO GLY ASP ASP THR PRO
SEQRES 14 A 394 ILE VAL ARG GLY SER ALA LEU LYS ALA LEU GLU GLY ASP
SEQRES 15 A 394 ALA GLU TRP GLU ALA LYS ILE LEU GLU LEU ALA GLY PHE
SEQRES 16 A 394 LEU ASP SER TYR ILE PRO GLU PRO GLU ARG ALA ILE ASP
SEQRES 17 A 394 LYS PRO PHE LEU LEU PRO ILE GLU ASP VAL PHE SER ILE
SEQRES 18 A 394 SER GLY ARG GLY THR VAL VAL THR GLY ARG VAL GLU ARG
SEQRES 19 A 394 GLY ILE ILE LYS VAL GLY GLU GLU VAL GLU ILE VAL GLY
SEQRES 20 A 394 ILE LYS GLU THR GLN LYS SER THR CYS THR GLY VAL GLU
SEQRES 21 A 394 MET PHE ARG LYS LEU LEU ASP GLU GLY ARG ALA GLY GLU
SEQRES 22 A 394 ASN VAL GLY VAL LEU LEU ARG GLY ILE LYS ARG GLU GLU
SEQRES 23 A 394 ILE GLU ARG GLY GLN VAL LEU ALA LYS PRO GLY THR ILE
SEQRES 24 A 394 LYS PRO HIS THR LYS PHE GLU SER GLU VAL TYR ILE LEU
SEQRES 25 A 394 SER LYS ASP GLU GLY GLY ARG HIS THR PRO PHE PHE LYS
SEQRES 26 A 394 GLY TYR ARG PRO GLN PHE TYR PHE ARG THR THR ASP VAL
SEQRES 27 A 394 THR GLY THR ILE GLU LEU PRO GLU GLY VAL GLU MET VAL
SEQRES 28 A 394 MET PRO GLY ASP ASN ILE LYS MET VAL VAL THR LEU ILE
SEQRES 29 A 394 HIS PRO ILE ALA MET ASP ASP GLY LEU ARG PHE ALA ILE
SEQRES 30 A 394 ARG GLU GLY GLY ARG THR VAL GLY ALA GLY VAL VAL ALA
SEQRES 31 A 394 LYS VAL LEU GLY
SEQRES 1 I 13 SER BB9 ASN BB6 H14 BB9 TYR 05N BB9 BB9 MH6 BB9 NH2
MODRES 4G5G BB9 I 901 CYS
MODRES 4G5G BB6 I 903 CYS (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID
MODRES 4G5G H14 I 904 PHE (2S,3R)-BETA-HYDROXY-PHENYLALANINE
MODRES 4G5G BB9 I 905 CYS
MODRES 4G5G 05N I 907 PRO (3R,4R)-4-HYDROXY-3-METHYL-L-PROLINE
MODRES 4G5G BB9 I 908 CYS
MODRES 4G5G BB9 I 909 CYS
MODRES 4G5G MH6 I 910 SER 3-HYDROXY-2-IMINOPROPANOIC ACID
MODRES 4G5G BB9 I 911 CYS
HET BB9 I 901 6
HET BB6 I 903 7
HET H14 I 904 11
HET BB9 I 905 6
HET 05N I 907 8
HET BB9 I 908 5
HET BB9 I 909 5
HET MH6 I 910 4
HET BB9 I 911 6
HET NH2 I 912 1
HET MG A 501 1
HET GDP A 502 28
HET MG A 503 1
HET SO4 A 504 5
HETNAM BB9 (2Z)-2-AMINO-3-SULFANYLPROP-2-ENOIC ACID
HETNAM BB6 (2Z)-2-AMINO-3-SULFANYLBUT-2-ENOIC ACID
HETNAM H14 (2S,3R)-BETA-HYDROXY-PHENYLALANINE
HETNAM 05N (3R,4R)-4-HYDROXY-3-METHYL-L-PROLINE
HETNAM MH6 3-HYDROXY-2-IMINOPROPANOIC ACID
HETNAM NH2 AMINO GROUP
HETNAM MG MAGNESIUM ION
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM SO4 SULFATE ION
HETSYN H14 BETA-HYDROXY-PHENYLALANINE, THREO-BETA-HYDROXY-L-
HETSYN 2 H14 PHENYLALANINE, (BETAS)-BETA-HYDROXY-L-PHENYLALANINE,
HETSYN 3 H14 L-THREO-3-PHENYLSERINE, L-THREO-BETA-PHENYLSERINE, 3-
HETSYN 4 H14 HYDROXY-L-PHENYLALANINE
FORMUL 2 BB9 5(C3 H5 N O2 S)
FORMUL 2 BB6 C4 H7 N O2 S
FORMUL 2 H14 C9 H11 N O3
FORMUL 2 05N C6 H11 N O3
FORMUL 2 MH6 C3 H5 N O3
FORMUL 2 NH2 H2 N
FORMUL 3 MG 2(MG 2+)
FORMUL 4 GDP C10 H15 N5 O11 P2
FORMUL 6 SO4 O4 S 2-
FORMUL 7 HOH *117(H2 O)
HELIX 1 1 GLY A 23 GLY A 40 1 18
HELIX 2 2 ALA A 45 ASN A 51 1 7
HELIX 3 3 GLY A 83 GLY A 94 1 12
HELIX 4 4 MET A 112 GLY A 126 1 15
HELIX 5 5 GLU A 144 TYR A 160 1 17
HELIX 6 6 SER A 173 GLU A 179 1 7
HELIX 7 7 ASP A 181 ILE A 199 1 19
HELIX 8 8 ARG A 204 LYS A 208 5 5
SHEET 1 A 6 SER A 65 ASP A 70 0
SHEET 2 A 6 HIS A 75 ASP A 80 -1 O HIS A 78 N VAL A 67
SHEET 3 A 6 HIS A 11 ILE A 17 1 N VAL A 14 O ALA A 77
SHEET 4 A 6 ALA A 101 ALA A 106 1 O ILE A 102 N GLY A 15
SHEET 5 A 6 ILE A 130 ASN A 135 1 O ILE A 131 N LEU A 103
SHEET 6 A 6 ILE A 169 ARG A 171 1 O VAL A 170 N VAL A 132
SHEET 1 B 2 GLU A 54 LYS A 56 0
SHEET 2 B 2 THR A 61 ASN A 63 -1 O ILE A 62 N GLU A 55
SHEET 1 C 7 LEU A 211 PRO A 213 0
SHEET 2 C 7 VAL A 291 ALA A 293 -1 O LEU A 292 N LEU A 212
SHEET 3 C 7 GLU A 241 VAL A 245 -1 N GLU A 243 O ALA A 293
SHEET 4 C 7 GLN A 251 MET A 260 -1 O GLN A 251 N ILE A 244
SHEET 5 C 7 ASN A 273 LEU A 278 -1 O LEU A 277 N GLY A 257
SHEET 6 C 7 GLY A 224 ARG A 230 -1 N VAL A 227 O VAL A 276
SHEET 7 C 7 VAL A 217 ILE A 220 -1 N PHE A 218 O VAL A 226
SHEET 1 D 5 LEU A 211 PRO A 213 0
SHEET 2 D 5 VAL A 291 ALA A 293 -1 O LEU A 292 N LEU A 212
SHEET 3 D 5 GLU A 241 VAL A 245 -1 N GLU A 243 O ALA A 293
SHEET 4 D 5 GLN A 251 MET A 260 -1 O GLN A 251 N ILE A 244
SHEET 5 D 5 LYS A 263 LEU A 265 -1 O LEU A 265 N VAL A 258
SHEET 1 E 2 ILE A 235 LYS A 237 0
SHEET 2 E 2 GLU A 267 ARG A 269 -1 O GLY A 268 N ILE A 236
SHEET 1 F 7 LYS A 299 ILE A 310 0
SHEET 2 F 7 ASN A 355 MET A 368 -1 O LEU A 362 N THR A 302
SHEET 3 F 7 THR A 335 GLU A 342 -1 N THR A 340 O THR A 361
SHEET 4 F 7 GLN A 329 PHE A 332 -1 N PHE A 330 O VAL A 337
SHEET 5 F 7 ARG A 373 GLU A 378 -1 O ALA A 375 N TYR A 331
SHEET 6 F 7 ARG A 381 GLY A 393 -1 O GLY A 386 N PHE A 374
SHEET 7 F 7 LYS A 299 ILE A 310 -1 N GLU A 305 O LYS A 390
SHEET 1 G 2 PHE A 322 PHE A 323 0
SHEET 2 G 2 MET A 349 VAL A 350 -1 O VAL A 350 N PHE A 322
LINK C SER I 900 N BB9 I 901 1555 1555 1.34
LINK C BB9 I 901 N ASN I 902 1555 1555 1.35
LINK C H14 I 904 N BB9 I 905 1555 1555 1.35
LINK C BB9 I 905 N TYR I 906 1555 1555 1.34
LINK C22 05N I 907 N BB9 I 908 1555 1555 1.30
LINK C BB9 I 908 N BB9 I 909 1555 1555 1.33
LINK C BB9 I 909 N MH6 I 910 1555 1555 1.35
LINK C MH6 I 910 N BB9 I 911 1555 1555 1.32
LINK C BB9 I 911 N NH2 I 912 1555 1555 1.33
LINK OG1 THR A 25 MG MG A 501 1555 1555 2.25
LINK MG MG A 501 O2B GDP A 502 1555 1555 2.31
LINK MG MG A 501 O HOH A 615 1555 1555 2.19
LINK MG MG A 503 O HOH A 654 1555 1555 2.33
LINK MG MG A 501 O HOH A 601 1555 1555 2.35
LINK MG MG A 501 O HOH A 602 1555 1555 2.41
LINK MG MG A 503 O HOH A 653 1555 1555 2.41
LINK MG MG A 501 O HOH A 616 1555 1555 2.42
LINK MG MG A 503 O HOH A 681 1555 1555 2.44
LINK C TYR I 906 N3 05N I 907 1555 1555 1.33
LINK CA SER I 900 C BB9 I 909 1555 1555 1.42
LINK CB SER I 900 CB MH6 I 910 1555 1555 1.43
LINK C BB9 I 908 SG BB9 I 909 1555 1555 1.74
LINK C SER I 900 SG BB9 I 901 1555 1555 1.75
LINK C H14 I 904 SG BB9 I 905 1555 1555 1.76
LINK C ASN I 902 SG BB6 I 903 1555 1555 1.77
LINK C MH6 I 910 SG BB9 I 911 1555 1555 1.77
LINK C22 05N I 907 SG BB9 I 908 1555 1555 1.76
SITE 1 AC1 7 THR A 25 CYS A 81 GDP A 502 HOH A 601
SITE 2 AC1 7 HOH A 602 HOH A 615 HOH A 616
SITE 1 AC2 19 ASP A 21 HIS A 22 GLY A 23 LYS A 24
SITE 2 AC2 19 THR A 25 THR A 26 PHE A 46 ASN A 135
SITE 3 AC2 19 LYS A 136 ASP A 138 MET A 139 SER A 173
SITE 4 AC2 19 ALA A 174 LEU A 175 MG A 501 HOH A 601
SITE 5 AC2 19 HOH A 602 HOH A 605 HOH A 615
SITE 1 AC3 4 GLU A 152 HOH A 653 HOH A 654 HOH A 681
SITE 1 AC4 5 ARG A 262 ARG A 318 HIS A 319 THR A 320
SITE 2 AC4 5 ARG A 381
SITE 1 AC5 18 GLU A 215 THR A 228 GLY A 257 GLU A 259
SITE 2 AC5 18 PHE A 261 ARG A 262 LEU A 264 ASN A 273
SITE 3 AC5 18 VAL A 274 GLY A 275 LEU A 277 THR A 320
SITE 4 AC5 18 PRO A 321 PHE A 323 LYS A 324 HOH A 672
SITE 5 AC5 18 HOH I1001 HOH I1002
CRYST1 80.305 123.577 45.092 90.00 90.00 90.00 P 21 21 2 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.012453 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008092 0.000000 0.00000
SCALE3 0.000000 0.000000 0.022177 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
